Biomedical subjects

Akio Nakamura

Publications and source records attributed to Akio Nakamura.

39 records · Page 3Linked to original sources

PubMed2002

Physiological incidents during 39 years of hypobaric chamber training in Japan.

BACKGROUND: Hypobaric chamber training for military aircrew is very important for flight safety. Since we began hypobaric training in our laboratory in 1960, some trainees have suffered physiological incidents. This study will characterize the physiological incidents during hypobaric chamber training at the Japan Air Self-Defense Force (JASDF). METHODS: All available training records from 1960-1998 were reviewed and the frequency of physiological incidents counted and analyzed. RESULTS: There were 29,677 trainees and 58,454 exposures. Overall frequency of physiological incidents was 6.3%. Physiological incidents included ear pain, paranasal sinus pain, abdominal pain, hypoxia, hyperventilation, joint pain, and toothache. Decompression sickness (DCS-I, simple joint pain only) was rare. In cases of DCS-I, joint pain was easily relieved with controlled descent. During the last three decades, overall prevalence of physiological incidents has gradually increased from 5.3 to approximately 6.1% before 1991, to 6.8-9.9% after 1991. However, prevalence rate showed no change through out the period when ear pain was factored out. The increase in prevalence was entirely due to an increased frequency of ear pain: 3.6 to approximately 4.6% before 1991, and 5.4 to approximately 7.2% after 1991. CONCLUSIONS: DCS has not been a problem in the JASDF hypobaric chamber training experience. The majority of physiological incidents during hypobaric chamber training in JASDF have been ear pain, a minor but frequent obstacle to hypobaric training. The exact cause of the observed increase in frequency of Eustachian tube dysfunction currently remains unclear.

Adult↗

PubMed2001

Activation of beta(2)-adrenoceptor prevents shiga toxin 2-induced TNF-alpha gene transcription.

Exposure of renal tubular epithelial cells to shiga toxin 2 (Stx-2) causes cytotoxicity, and the potency of this toxin is enhanced in the presence of tumor necrosis factor-alpha (TNF-alpha). It has been shown that Stx-2 induces TNF-alpha production and that activation of beta(2)-adrenoceptors downregulates TNF-alpha. However, little is known about the signaling pathway by which beta(2)-adrenoceptor agonists suppress the Stx-2-induced TNF-alpha gene transcription. The possible signaling components involved in this pathway were investigated. Human adenocarcinoma-derived renal tubular epithelial cells (ACHN) were exposed to Stx-2 in the presence or absence of a beta(2)-adrenoceptor agonist. Mitogen-activated protein kinase (MAPK), activating protein-1 (AP-1), and nuclear factor-kappa B (NF-kappa B) were measured to evaluate the regulatory mechanisms involved in TNF-alpha gene transcription. Stx-2 (4 pg/ml) stimulated MAPK (p42/p44, p38) and AP-1 and increased TNF-alpha promoter activity by 2.4-fold. The increase in TNF-alpha was attenuated by both a p42/p44 inhibitor, PD098059 (10(-6) M), and a p38 inhibitor, SB203580 (10(-6) M), and AP-1-binding activity was inhibited by PD098059. Terbutaline (10(-6) M to 10(-8) M) suppressed MAPK (p42/p44, p38), NF-kappa B (p50, p65), and TNF-alpha promoter activity in a dose-dependent way that was prevented by the beta(2)-adrenoceptor antagonist, ICI118,551. However, inhibition of MAPK (p42/p44) and TNF-alpha promoter activity was partially prevented by the cAMP-protein kinase (PKA) inhibitors, H-89 (5 x 10(-6) M) and KT5720 (10(-5) M), whereas the suppression of p38 MAPK or NF-kappa B (p50) was not blocked by these inhibitors. The suppression of NF-kappa B (p65) was completely overcome by H-89 or KT5720. In summary, the downregulation of TNF-alpha transcription by terbutaline was mediated by an inhibitory effect of beta(2)-adrenoceptor activation on MAPK (p42/p44, p38) and NF-kappa B (p50/p65), which were exerted through a cAMP-PKA pathway and a cAMP-independent mechanism. It is likely that cAMP-PKA and MAPK (p42/p44, p38) may play a critical role in the regulation of the Stx-2-induced TNF-alpha transcription via beta(2)-adrenoceptor activation.

Adrenergic beta-Agonists↗

PubMedDate not supplied

The specificity of lipoxygenase-catalyzed lipid peroxidation and the effects of radical-scavenging antioxidants.

The oxidation of low density lipoprotein (LDL) by lipoxygenase has been implicated in the pathogenesis of atherosclerosis. It has been known that lipoxygenase-mediated lipid peroxidation proceeds in general via regio-, stereo- and enantio-specific mechanisms, but that it is sometimes accompanied by a share of random hydroperoxides as side reaction products. In this study we investigated the oxidation of various substrates (linoleic acid, methyl linoleate, phosphatidylcholine, isolated LDL, and human plasma) by the arachidonate 15-lipoxygenases from rabbit reticulocytes and soybeans aiming at elucidating the effects of substrate, lipoxygenase and reaction milieu on the contribution and mechanism of random oxidation and also the effect of antioxidant. The specific character of the rabbit 15-lipoxygenase reaction was confirmed under all conditions employed here. However, the specificity by soybean lipoxygenase was markedly dependent on the conditions. When phosphatidylcholine liposomes and LDL were oxygenated by soybean lipoxygenase, the product pattern was found to be exclusively regio-, stereo-, and enantio-random. When free linoleic acid was incorporated into PC liposomes and oxidized by soybean lipoxygenase, the free acid was specifically oxygenated, whereas esterified linoleate gave random oxidation products exclusively. Radical-scavenging antioxidants such as alpha-tocopherol, ascorbic acid and 2-carboxy-2,5,7,8-tetramethyl-6-chromanol selectively inhibited the random oxidation but did not influence specific product formation. It is assumed that the random reaction products originate from free radical intermediates, which have escaped the active site of the enzyme and thus may be accessible to radical scavengers. These data indicate that the specificity of lipoxygenase-catalyzed lipid oxidation and the inhibitory effects of antioxidants depend on the physico-chemical state of the substrate and type of lipoxygenase and that they may change completely depending on the conditions.

Animals↗